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Article ; Online: Peptidomics Analysis of Milk Protein-Derived Peptides Released over Time in the Preterm Infant Stomach.

Beverly, Robert L / Underwood, Mark A / Dallas, David C

2019 Volume 18, Issue 3, Page(s) 912–922

Abstract: Over the course of milk digestion, native milk proteases and infant digestive proteases fragment intact proteins into peptides with potential bioactivity. This study investigated the release of peptides over 3 h of gastric digestion in 14 preterm infant ... ...

Abstract	Over the course of milk digestion, native milk proteases and infant digestive proteases fragment intact proteins into peptides with potential bioactivity. This study investigated the release of peptides over 3 h of gastric digestion in 14 preterm infant sample sets. The peptide content was extracted and analyzed from milk and gastric samples via Orbitrap tandem mass spectrometry. The relative ion intensity (abundance) and count of peptides in each sample were compared over time and between infants fed milk fortified with bovine milk fortifier and infants fed unfortified milk. Bioactivity of the identified peptides was predicted by sequence homology to known bioactive milk peptides. Both total and bioactive peptide abundance and count continuously increased over 3 h of gastric digestion. After accounting for infant weight, length, and postconceptual age, fortification of milk limited the release of peptides from human milk proteins. Peptides that survived further gastric digestion after their initial release were structurally more similar to bioactive peptides than nonsurviving peptides. This work is the first to provide a comprehensive profile of milk peptides released during gastric digestion over time, which is an essential step in determining which peptides are most likely to be biologically relevant in the infant. Data are available via ProteomeXchange with identifier PXD012192.
MeSH term(s)	Animals ; Cattle ; Gastric Mucosa/metabolism ; Humans ; Infant ; Infant, Newborn ; Infant, Premature/metabolism ; Milk Proteins/metabolism ; Milk, Human/chemistry ; Peptides/analysis ; Proteomics/methods ; Stomach ; Tandem Mass Spectrometry
Chemical Substances	Milk Proteins ; Peptides
Language	English
Publishing date	2019-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.8b00604
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Article ; Online: Differences and Similarities in the Peptide Profile of Preterm and Term Mother's Milk, and Preterm and Term Infant Gastric Samples.

Nielsen, Søren D / Beverly, Robert L / Underwood, Mark A / Dallas, David C

Nutrients

2020 Volume 12, Issue 9

Abstract: Our previous studies revealed that milk proteases begin to hydrolyze proteins in the mammary gland and that proteolytic digestion continues within the infant stomach. No research has measured how the release of milk peptides differs between the gastric ... ...

Abstract	Our previous studies revealed that milk proteases begin to hydrolyze proteins in the mammary gland and that proteolytic digestion continues within the infant stomach. No research has measured how the release of milk peptides differs between the gastric aspirates of term and premature infants. This study examined the presence of milk peptides in milk and gastric samples from term and preterm infants using an Orbitrap Fusion Lumos mass spectrometer. Samples were collected from nine preterm-delivering and four term-delivering mother-infant pairs. Our study reveals an increased count and ion abundance of peptides and decreased peptide length from mother's milk to the infant stomach, confirming that additional break-down of the milk proteins occurred in both preterm and term infants' stomachs. Protein digestion occurred at a higher level in the gastric contents of term infants than in gastric contents of preterm infants. An amino acid cleavage site-based enzyme analysis suggested that the observed higher proteolysis in the term infants was due to higher pepsin/cathepsin D activity in the stomach. Additionally, there was a higher quantity of antimicrobial peptides in term infant gastric contents than in those of preterm infants, which could indicate that preterm infants benefit less from bioactive peptides in the gut.
MeSH term(s)	Adolescent ; Adult ; Female ; Gastric Mucosa ; Gastrointestinal Contents/chemistry ; Humans ; Infant ; Infant, Newborn ; Infant, Premature ; Milk, Human/chemistry ; Mothers ; Peptides/analysis ; Stomach ; Young Adult
Chemical Substances	Peptides
Language	English
Publishing date	2020-09-15
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2518386-2
ISSN	2072-6643 ; 2072-6643
ISSN (online)	2072-6643
ISSN	2072-6643
DOI	10.3390/nu12092825
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Article ; Online: Release of functional peptides from mother's milk and fortifier proteins in the premature infant stomach.

Nielsen, Søren D / Beverly, Robert L / Underwood, Mark A / Dallas, David C

PloS one

2018 Volume 13, Issue 11, Page(s) e0208204

Abstract: Digestion of milk proteins in the premature infant stomach releases functional peptides; however, which peptides are present has not been reported. Premature infants are often fed a combination of human milk and bovine milk fortifiers, but the variety of ...

Abstract	Digestion of milk proteins in the premature infant stomach releases functional peptides; however, which peptides are present has not been reported. Premature infants are often fed a combination of human milk and bovine milk fortifiers, but the variety of functional peptides released from both human and bovine milk proteins remains uncharacterized. This study applied peptidomics to investigate the peptides released in gastric digestion of mother's milk proteins and supplemental bovine milk proteins in premature infants. Peptides were assessed for homology against a database of known functional peptides-Milk Bioactive Peptide Database. The peptidomic data were analyzed to interpret which proteases most likely released them from the parent protein. We identified 5,264 unique peptides from bovine and human milk proteins within human milk, fortifier or infant gastric samples. Plasmin was predicted to be the most active protease in milk, while pepsin or cathepsin D were predicted to be most active in the stomach. Alignment of the peptide distribution showed a different digestion pattern between human and bovine proteins. The number of peptides with high homology to known functional peptides (antimicrobial, angiotensin-converting enzyme-inhibitory, antioxidant, immunomodulatory, etc.) increased from milk to the premature infant stomach and was greater from bovine milk proteins than human milk proteins. The differential release of bioactive peptides from human and bovine milk proteins may impact overall health outcomes in premature infants.
MeSH term(s)	Adult ; Amino Acid Sequence ; Animals ; Cattle ; Female ; Gastric Mucosa/metabolism ; Humans ; Infant, Premature/metabolism ; Male ; Milk Proteins/analysis ; Milk Proteins/metabolism ; Milk, Human/chemistry ; Milk, Human/metabolism ; Peptide Mapping ; Peptides/analysis ; Peptides/metabolism ; Spectrometry, Mass, Electrospray Ionization
Chemical Substances	Milk Proteins ; Peptides
Language	English
Publishing date	2018-11-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0208204
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Article: Peptidomics Analysis of Milk Protein-Derived Peptides Released over Time in the Preterm Infant Stomach

Beverly, Robert L / Underwood, Mark A / Dallas, David C

Journal of proteome research. 2019 Jan. 14, v. 18, no. 3

2019

Abstract	Over the course of milk digestion, native milk proteases and infant digestive proteases fragment intact proteins into peptides with potential bioactivity. This study investigated the release of peptides over 3 h of gastric digestion in 14 preterm infant sample sets. The peptide content was extracted and analyzed from milk and gastric samples via Orbitrap tandem mass spectrometry. The relative ion intensity (abundance) and count of peptides in each sample were compared over time and between infants fed milk fortified with bovine milk fortifier and infants fed unfortified milk. Bioactivity of the identified peptides was predicted by sequence homology to known bioactive milk peptides. Both total and bioactive peptide abundance and count continuously increased over 3 h of gastric digestion. After accounting for infant weight, length, and postconceptual age, fortification of milk limited the release of peptides from human milk proteins. Peptides that survived further gastric digestion after their initial release were structurally more similar to bioactive peptides than nonsurviving peptides. This work is the first to provide a comprehensive profile of milk peptides released during gastric digestion over time, which is an essential step in determining which peptides are most likely to be biologically relevant in the infant. Data are available via ProteomeXchange with identifier PXD012192.
Keywords	bioactive properties ; digestion ; human milk proteins ; infants ; milk ; peptides ; premature birth ; proteinases ; proteome ; sequence homology ; stomach ; tandem mass spectrometry
Language	English
Dates of publication	2019-0114
Size	p. 912-922.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.8b00604
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Comparison of Human Milk Immunoglobulin Survival during Gastric Digestion between Preterm and Term Infants.

Demers-Mathieu, Veronique / Underwood, Mark A / Beverly, Robert L / Nielsen, Søren D / Dallas, David C

Nutrients

2018 Volume 10, Issue 5

Abstract: Human milk provides immunoglobulins (Igs) that supplement the passive immune system of neonates; however, the extent of survival of these Igs during gastric digestion and whether this differs between preterm and term infants remains unknown. Human milk, ... ...

Abstract	Human milk provides immunoglobulins (Igs) that supplement the passive immune system of neonates; however, the extent of survival of these Igs during gastric digestion and whether this differs between preterm and term infants remains unknown. Human milk, and infant gastric samples at 2 h post-ingestion were collected from 15 preterm (23⁻32 week gestational age (GA)) mother-infant pairs and from 8 term (38⁻40 week of GA) mother-infant pairs within 7⁻98 days postnatal age. Samples were analyzed via ELISA for concentration of total IgA (secretory IgA (SIgA)/IgA), total secretory component (SC/SIgA/SIgM), total IgM (SIgM/IgM), and IgG as well as peptidomics. Total IgA concentration decreased by 60% from human milk to the preterm infant stomach and decreased by 48% in the term infant stomach. Total IgM and IgG concentrations decreased by 33% and 77%, respectively, from human milk to the term infant stomach but were stable in the preterm infant stomach. Release of peptides from all Ig isotypes in the term infant stomach was higher than in the preterm stomach. Overall, the stability of human milk Igs during gastric digestion is higher in preterm infant than in term infants, which could be beneficial for assisting the preterm infants' immature immune system.
MeSH term(s)	Digestion ; Drug Stability ; Female ; Gastric Mucosa/metabolism ; Gestational Age ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin A/analysis ; Immunoglobulin A, Secretory/analysis ; Immunoglobulin G/analysis ; Immunoglobulin M/analysis ; Immunoglobulins/metabolism ; Infant ; Infant, Newborn ; Infant, Premature/metabolism ; Milk, Human/immunology ; Peptides/analysis ; Secretory Component/analysis ; Stomach/immunology
Chemical Substances	Immunoglobulin A ; Immunoglobulin A, Secretory ; Immunoglobulin G ; Immunoglobulin M ; Immunoglobulins ; Peptides ; Secretory Component
Language	English
Publishing date	2018-05-17
Publishing country	Switzerland
Document type	Comparative Study ; Journal Article
ZDB-ID	2518386-2
ISSN	2072-6643 ; 2072-6643
ISSN (online)	2072-6643
ISSN	2072-6643
DOI	10.3390/nu10050631
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Article ; Online: Survival of Immunoglobulins from Human Milk to Preterm Infant Gastric Samples at 1, 2, and 3 h Postprandial.

Demers-Mathieu, Veronique / Underwood, Mark A / Beverly, Robert L / Dallas, David C

Neonatology

2018 Volume 114, Issue 3, Page(s) 242–250

Abstract: Background: Human milk immunoglobulins (Ig) are an important support for the naïve infant immune system; yet the extent to which these proteins survive within the infant digestive tract, particularly for preterm infants, is poorly studied.: Objectives! ...

Abstract	Background: Human milk immunoglobulins (Ig) are an important support for the naïve infant immune system; yet the extent to which these proteins survive within the infant digestive tract, particularly for preterm infants, is poorly studied. Objectives: Our objective was to evaluate the survival of human milk Igs in the preterm stomach across postprandial time. Methods: Human milk and infant gastric samples were collected from 11 preterm (23-32 weeks gestational age) mother-infant pairs within 7-98 days postnatal age. Preterm gastric samples were collected 1, 2, and 3 h after the beginning of the feeding. Samples were analyzed for concentration of total IgA (secretory IgA [SIgA]/IgA), total secretory component (SC/SIgA/SIgM), total IgM (SIgM/IgM), and IgG via enzyme-linked immunosorbent assay. Ig-chain fragment peptides were determined using peptidomic analysis. One-way analysis of variance with repeated measures followed by Tukey's multiple comparison tests was applied. Results: Concentrations of total IgA were lower in the gastric contents at 3 h postprandial compared with human milk and gastric contents at 1 and 2 h. Human milk SC/SIgA/SIgM, IgG, and total IgM concentrations remained stable in the preterm stomach across postprandial time. Peptide counts from the Ig alpha-chain and the Ig gamma-chain increased in gastric contents from 1 to 2 h postprandial. Peptide counts from the human milk Ig-chain, Ig-chain, and SC were stable across postprandial time. These peptides from Ig-chains were not present in human milk but were released in the stomach due to their partial degradation. Conclusions: Human milk total SC (SIgA/SC/SIgM), total IgM, and IgG survived mostly intact through the preterm infant stomach, while total IgA was -partially digested.
MeSH term(s)	Analysis of Variance ; Digestion ; Female ; Gastric Mucosa/metabolism ; Gestational Age ; Humans ; Immunoglobulin A/analysis ; Immunoglobulin G/analysis ; Immunoglobulin M/analysis ; Immunoglobulins/analysis ; Infant ; Infant, Newborn ; Infant, Premature/metabolism ; Male ; Milk, Human/immunology ; Peptides/analysis ; Protein Stability ; Secretory Component/analysis ; Stomach/immunology
Chemical Substances	Immunoglobulin A ; Immunoglobulin G ; Immunoglobulin M ; Immunoglobulins ; Peptides ; Secretory Component
Language	English
Publishing date	2018-06-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2266911-5
ISSN	1661-7819 ; 1661-7800
ISSN (online)	1661-7819
ISSN	1661-7800
DOI	10.1159/000489387
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Article ; Online: Ribovore: ribosomal RNA sequence analysis for GenBank submissions and database curation.

Schäffer, Alejandro A / McVeigh, Richard / Robbertse, Barbara / Schoch, Conrad L / Johnston, Anjanette / Underwood, Beverly A / Karsch-Mizrachi, Ilene / Nawrocki, Eric P

BMC bioinformatics

2021 Volume 22, Issue 1, Page(s) 400

Abstract: Background: The DNA sequences encoding ribosomal RNA genes (rRNAs) are commonly used as markers to identify species, including in metagenomics samples that may combine many organismal communities. The 16S small subunit ribosomal RNA (SSU rRNA) gene is ... ...

Abstract	Background: The DNA sequences encoding ribosomal RNA genes (rRNAs) are commonly used as markers to identify species, including in metagenomics samples that may combine many organismal communities. The 16S small subunit ribosomal RNA (SSU rRNA) gene is typically used to identify bacterial and archaeal species. The nuclear 18S SSU rRNA gene, and 28S large subunit (LSU) rRNA gene have been used as DNA barcodes and for phylogenetic studies in different eukaryote taxonomic groups. Because of their popularity, the National Center for Biotechnology Information (NCBI) receives a disproportionate number of rRNA sequence submissions and BLAST queries. These sequences vary in quality, length, origin (nuclear, mitochondria, plastid), and organism source and can represent any region of the ribosomal cistron. Results: To improve the timely verification of quality, origin and loci boundaries, we developed Ribovore, a software package for sequence analysis of rRNA sequences. The ribotyper and ribosensor programs are used to validate incoming sequences of bacterial and archaeal SSU rRNA. The ribodbmaker program is used to create high-quality datasets of rRNAs from different taxonomic groups. Key algorithmic steps include comparing candidate sequences against rRNA sequence profile hidden Markov models (HMMs) and covariance models of rRNA sequence and secondary-structure conservation, as well as other tests. Nine freely available blastn rRNA databases created and maintained with Ribovore are used for checking incoming GenBank submissions and used by the blastn browser interface at NCBI. Since 2018, Ribovore has been used to analyze more than 50 million prokaryotic SSU rRNA sequences submitted to GenBank, and to select at least 10,435 fungal rRNA RefSeq records from type material of 8350 taxa. Conclusion: Ribovore combines single-sequence and profile-based methods to improve GenBank processing and analysis of rRNA sequences. It is a standalone, portable, and extensible software package for the alignment, classification and validation of rRNA sequences. Researchers planning on submitting SSU rRNA sequences to GenBank are encouraged to download and use Ribovore to analyze their sequences prior to submission to determine which sequences are likely to be automatically accepted into GenBank.
MeSH term(s)	DNA, Ribosomal ; Databases, Nucleic Acid ; Phylogeny ; RNA, Ribosomal ; RNA, Ribosomal, 16S/genetics ; RNA, Ribosomal, 18S/genetics ; Sequence Analysis, RNA
Chemical Substances	DNA, Ribosomal ; RNA, Ribosomal ; RNA, Ribosomal, 16S ; RNA, Ribosomal, 18S
Language	English
Publishing date	2021-08-12
Publishing country	England
Document type	Journal Article
ZDB-ID	2041484-5
ISSN	1471-2105 ; 1471-2105
ISSN (online)	1471-2105
ISSN	1471-2105
DOI	10.1186/s12859-021-04316-z
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Article: Differences and Similarities in the Peptide Profile of Preterm and Term Mother’s Milk, and Preterm and Term Infant Gastric Samples

Nielsen, Søren D / Beverly, Robert L / Underwood, Mark A / Dallas, David C

Nutrients. 2020 Sept. 15, v. 12, no. 9

2020

Abstract	Our previous studies revealed that milk proteases begin to hydrolyze proteins in the mammary gland and that proteolytic digestion continues within the infant stomach. No research has measured how the release of milk peptides differs between the gastric aspirates of term and premature infants. This study examined the presence of milk peptides in milk and gastric samples from term and preterm infants using an Orbitrap Fusion Lumos mass spectrometer. Samples were collected from nine preterm-delivering and four term-delivering mother–infant pairs. Our study reveals an increased count and ion abundance of peptides and decreased peptide length from mother’s milk to the infant stomach, confirming that additional break-down of the milk proteins occurred in both preterm and term infants’ stomachs. Protein digestion occurred at a higher level in the gastric contents of term infants than in gastric contents of preterm infants. An amino acid cleavage site-based enzyme analysis suggested that the observed higher proteolysis in the term infants was due to higher pepsin/cathepsin D activity in the stomach. Additionally, there was a higher quantity of antimicrobial peptides in term infant gastric contents than in those of preterm infants, which could indicate that preterm infants benefit less from bioactive peptides in the gut.
Keywords	amino acids ; antimicrobial peptides ; cathepsins ; digestion ; length ; mammary glands ; milk ; pepsin ; proteolysis ; research ; spectrometers ; stomach
Language	English
Dates of publication	2020-0915
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
Note	NAL-light
ZDB-ID	2518386-2
ISSN	2072-6643
ISSN	2072-6643
DOI	10.3390/nu12092825
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Article ; Online: Rapid automated validation, annotation and publication of SARS-CoV-2 sequences to GenBank.

Underwood, Beverly A / Yankie, Linda / Nawrocki, Eric P / Palanigobu, Vasuki / Gotvyanskyy, Sergiy / Calhoun, Vincent C / Kornbluh, Michael / Smith, Thomas G / Fleischmann, Lydia / Sinyakov, Denis / Bollin, Colleen J / Karsch-Mizrachi, Ilene

Database : the journal of biological databases and curation

2022 Volume 2022

Abstract: Rapid response to the current coronavirus disease 2019 (COVID-19) pandemic requires fast dissemination of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genomic sequence data in order to align diagnostic tests and vaccines with the natural ... ...

Abstract	Rapid response to the current coronavirus disease 2019 (COVID-19) pandemic requires fast dissemination of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genomic sequence data in order to align diagnostic tests and vaccines with the natural evolution of the virus as it spreads through the world. To facilitate this, the National Library of Medicine's National Center for Biotechnology Information developed an automated pipeline for the deposition and quick processing of SARS-CoV-2 genome assemblies into GenBank for the user community. The pipeline ensures the collection of contextual information about the virus source, assesses sequence quality and annotates descriptive biological features, such as protein-coding regions and mature peptides. The process promotes standardized nomenclature and creates and publishes fully processed GenBank files within minutes of deposition. The software has processed and published 982 454 annotated SARS-CoV-2 sequences, as of 21 October 2021. This development addresses the needs of the scientific community as the sequencing of SARS-CoV-2 genomes increases and will facilitate unrestricted access to and usability of SARS-CoV-2 genomic sequence data, providing important reagents for scientific and public health activities in response to the COVID-19 pandemic. Database URL https://submit.ncbi.nlm.nih.gov/sarscov2/genbank/.
MeSH term(s)	COVID-19/epidemiology ; COVID-19/genetics ; Databases, Nucleic Acid ; Genome, Viral/genetics ; Humans ; Pandemics ; SARS-CoV-2/genetics
Language	English
Publishing date	2022-03-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2496706-3
ISSN	1758-0463 ; 1758-0463
ISSN (online)	1758-0463
ISSN	1758-0463
DOI	10.1093/database/baac006
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Article ; Online: Follow-up Schedule for Patients With Sentinel Node-negative Cutaneous Melanoma (The MELFO Study): An International Phase III Randomized Clinical Trial.

Moncrieff, Marc D / Bastiaannet, Esther / Underwood, Beverly / Francken, Anne Brecht / Garioch, Jennifer / Damude, Samantha / Heaton, Martin / Deckers, Eric A / Patel, Nakul / Hoekstra-Weebers, Josette E / Hoekstra, Harald J

Annals of surgery

2022 Volume 276, Issue 4, Page(s) e208–e216

Abstract: Objectives and design: The MELFO (MELanoma FOllow-up) study is an international phase III randomized controlled trial comparing an experimental low-intensity schedule against current national guidelines.: Background: Evidence-based guidelines for the ...

Abstract	Objectives and design: The MELFO (MELanoma FOllow-up) study is an international phase III randomized controlled trial comparing an experimental low-intensity schedule against current national guidelines. Background: Evidence-based guidelines for the follow-up of sentinel node-negative melanoma patients are lacking. Methods: Overall, 388 adult patients diagnosed with sentinel node-negative primary melanoma patients were randomized in cancer centers in the Netherlands and United Kingdom between 2006 and 2016. The conventional schedule group (control: n=196) was reviewed as per current national guidelines. The experimental schedule group (n=192) was reviewed in a reduced-frequency schedule. Quality of life was the primary outcome measurement. Detection rates and survival outcomes were recorded. Patient satisfaction rates and compliance with allocated schedules were compared. Results: At 5 years, both arms expressed high satisfaction with their regimens (>97%). This study found no significant group effect on any patient-reported outcome measure scores between the follow-up protocols. In total, 75/388 (19.4%) patients recurred, with no difference in incidence found between the 2 arms (hazard ratio=0.87, 95% confidence interval: 0.54-1.39, P =0.57). Self-examination was the method of detection for 25 experimental patients and 32 control patients (75.8% vs. 76.2%; P =0.41). This study found no difference in any survival outcomes between the 2 study arms (disease-free survival: hazard ratio=1.00, 95% confidence interval: 0.49-2.07, P =0.99). Conclusions: A reduced-intensity, American Joint Committee on Cancer (AJCC) stage-adjusted follow-up schedule for sentinel node-negative melanoma patients is a safe strategy, and patient self-examination is effective for recurrence detection with no evidence of diagnostic delay. Patients' acceptance is very high.
MeSH term(s)	Adult ; Delayed Diagnosis ; Follow-Up Studies ; Humans ; Melanoma/pathology ; Neoplasm Staging ; Quality of Life ; Sentinel Lymph Node Biopsy ; Skin Neoplasms/pathology ; Melanoma, Cutaneous Malignant
Language	English
Publishing date	2022-07-22
Publishing country	United States
Document type	Clinical Trial, Phase III ; Journal Article ; Randomized Controlled Trial ; Research Support, Non-U.S. Gov't
ZDB-ID	340-2
ISSN	1528-1140 ; 0003-4932
ISSN (online)	1528-1140
ISSN	0003-4932
DOI	10.1097/SLA.0000000000005621
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